ES2550362T3 - Nuevas asparaginasas y usos de las mismas - Google Patents

Nuevas asparaginasas y usos de las mismas Download PDF

Info

Publication number: ES2550362T3
Authority: ES; Spain
Prior art keywords: ser; val; wing; thr; seq
Prior art date: 2007-04-20
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Active

Application number

ES08736346.1T

Other languages

English (en)

Spanish (es)

Inventor

Van Der Jan Metske Laan

Mark Cristiaan Stor

De Ilse Lange

Lisette Mohrmann

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

DSM IP Assets BV

Original Assignee

DSM IP Assets BV

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2007-04-20

Filing date

2008-04-17

Publication date

2015-11-06

2008-04-17 Application filed by DSM IP Assets BV filed Critical DSM IP Assets BV

2015-11-06 Application granted granted Critical

2015-11-06 Publication of ES2550362T3 publication Critical patent/ES2550362T3/es

Status Active legal-status Critical Current

2028-04-17 Anticipated expiration legal-status Critical

Links

102000015790 Asparaginase Human genes 0.000 title abstract description 18
108010024976 Asparaginase Proteins 0.000 title abstract description 18
229960003272 asparaginase Drugs 0.000 title abstract description 16
DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 title abstract description 16
108090000765 processed proteins & peptides Proteins 0.000 abstract description 37
229920001184 polypeptide Polymers 0.000 abstract description 35
102000004196 processed proteins & peptides Human genes 0.000 abstract description 35
150000007523 nucleic acids Chemical group 0.000 abstract description 33
FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 abstract description 22
108091028043 Nucleic acid sequence Proteins 0.000 abstract description 17
125000003275 alpha amino acid group Chemical group 0.000 abstract description 9
230000000694 effects Effects 0.000 abstract description 7
102000004190 Enzymes Human genes 0.000 abstract description 2
108090000790 Enzymes Proteins 0.000 abstract description 2
229940088598 enzyme Drugs 0.000 abstract description 2
102000039446 nucleic acids Human genes 0.000 description 26
108020004707 nucleic acids Proteins 0.000 description 26
108091033319 polynucleotide Proteins 0.000 description 17
102000040430 polynucleotide Human genes 0.000 description 17
239000002157 polynucleotide Substances 0.000 description 17
150000001413 amino acids Chemical class 0.000 description 16
239000013598 vector Substances 0.000 description 14
108020004414 DNA Proteins 0.000 description 13
108090000623 proteins and genes Proteins 0.000 description 12
230000000295 complement effect Effects 0.000 description 9
239000012634 fragment Substances 0.000 description 9
238000009396 hybridization Methods 0.000 description 7
125000003729 nucleotide group Chemical group 0.000 description 7
238000006467 substitution reaction Methods 0.000 description 6
239000013604 expression vector Substances 0.000 description 5
239000002773 nucleotide Substances 0.000 description 5
102000004169 proteins and genes Human genes 0.000 description 5
108020004511 Recombinant DNA Proteins 0.000 description 4
239000002299 complementary DNA Substances 0.000 description 4
238000000746 purification Methods 0.000 description 4
108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
108091026890 Coding region Proteins 0.000 description 3
230000037430 deletion Effects 0.000 description 3
238000012217 deletion Methods 0.000 description 3
230000006870 function Effects 0.000 description 3
230000004927 fusion Effects 0.000 description 3
230000037431 insertion Effects 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000003993 interaction Effects 0.000 description 3
230000010076 replication Effects 0.000 description 3
238000005406 washing Methods 0.000 description 3
102000053602 DNA Human genes 0.000 description 2
108010093488 His-His-His-His-His-His Proteins 0.000 description 2
108091034117 Oligonucleotide Proteins 0.000 description 2
108091034057 RNA (poly(A)) Proteins 0.000 description 2
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
230000001580 bacterial effect Effects 0.000 description 2
230000008827 biological function Effects 0.000 description 2
238000007796 conventional method Methods 0.000 description 2
108020001507 fusion proteins Proteins 0.000 description 2
102000037865 fusion proteins Human genes 0.000 description 2
239000003550 marker Substances 0.000 description 2
239000000463 material Substances 0.000 description 2
239000011159 matrix material Substances 0.000 description 2
108020004999 messenger RNA Proteins 0.000 description 2
238000000034 method Methods 0.000 description 2
230000035772 mutation Effects 0.000 description 2
239000013612 plasmid Substances 0.000 description 2
108091008146 restriction endonucleases Proteins 0.000 description 2
230000003612 virological effect Effects 0.000 description 2
AQVYQEWAZCIHMU-UHFFFAOYSA-N 1-[2-(4-fluorophenyl)-1,3-thiazol-5-yl]-1-pyridin-4-ylethanol Chemical compound C=1C=NC=CC=1C(O)(C)C(S1)=CN=C1C1=CC=C(F)C=C1 AQVYQEWAZCIHMU-UHFFFAOYSA-N 0.000 description 1
102000002260 Alkaline Phosphatase Human genes 0.000 description 1
108020004774 Alkaline Phosphatase Proteins 0.000 description 1
241000228245 Aspergillus niger Species 0.000 description 1
101000765308 Aspergillus niger N-(5'-phosphoribosyl)anthranilate isomerase Proteins 0.000 description 1
108020004635 Complementary DNA Proteins 0.000 description 1
HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
101710154606 Hemagglutinin Proteins 0.000 description 1
UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
229930010555 Inosine Natural products 0.000 description 1
101710163270 Nuclease Proteins 0.000 description 1
101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
238000012408 PCR amplification Methods 0.000 description 1
101710176177 Protein A56 Proteins 0.000 description 1
241000700605 Viruses Species 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
230000004075 alteration Effects 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
230000003321 amplification Effects 0.000 description 1
230000000692 anti-sense effect Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
239000012707 chemical precursor Substances 0.000 description 1
230000000052 comparative effect Effects 0.000 description 1
238000004590 computer program Methods 0.000 description 1
230000029087 digestion Effects 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
239000003797 essential amino acid Substances 0.000 description 1
235000020776 essential amino acid Nutrition 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
NLFLXLJXEIUQDL-UHFFFAOYSA-N gusacitinib Chemical compound C1CC(O)CCN1C(C=C1)=CC=C1NC1=NC(N2CCC(CC#N)CC2)=NC2=C1C(=O)NN=C2 NLFLXLJXEIUQDL-UHFFFAOYSA-N 0.000 description 1
206010022000 influenza Diseases 0.000 description 1
229960003786 inosine Drugs 0.000 description 1
230000013011 mating Effects 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
238000003199 nucleic acid amplification method Methods 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
238000000163 radioactive labelling Methods 0.000 description 1
230000037432 silent mutation Effects 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
239000001509 sodium citrate Substances 0.000 description 1
NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
239000000126 substance Substances 0.000 description 1
239000013603 viral vector Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
- C12N9/82—Asparaginase (3.5.1.1)
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/06—Enzymes
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
- A23L5/25—Removal of unwanted matter, e.g. deodorisation or detoxification using enzymes
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y305/00—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5)
- C12Y305/01—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5) in linear amides (3.5.1)
- C12Y305/01001—Asparaginase (3.5.1.1)

Landscapes

Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Microbiology (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Nutrition Science (AREA)
Polymers & Plastics (AREA)
Food Science & Technology (AREA)
Medicinal Chemistry (AREA)
Biotechnology (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
Pharmacology & Pharmacy (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Animal Behavior & Ethology (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Veterinary Medicine (AREA)
Public Health (AREA)
Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)
Coloring Foods And Improving Nutritive Qualities (AREA)

ES08736346.1T 2007-04-20 2008-04-17 Nuevas asparaginasas y usos de las mismas Active ES2550362T3 (es)

Applications Claiming Priority (7)

Application Number	Priority Date	Filing Date	Title
EP07106660		2007-04-20
EP07106662		2007-04-20
EP07106664		2007-04-20
EP07106662		2007-04-20
EP07106660		2007-04-20
EP07106664		2007-04-20
PCT/EP2008/054693 WO2008128975A1 (en)	2007-04-20	2008-04-17	Novel asparaginases and uses thereof

Publications (1)

Publication Number	Publication Date
ES2550362T3 true ES2550362T3 (es)	2015-11-06

Family

ID=39650693

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
ES08736346.1T Active ES2550362T3 (es)	2007-04-20	2008-04-17	Nuevas asparaginasas y usos de las mismas

Country Status (14)

Country	Link
US (3)	US20100136169A1 (ru)
EP (1)	EP2137306B1 (ru)
JP (1)	JP2010524448A (ru)
AR (1)	AR066410A1 (ru)
AU (1)	AU2008240797A1 (ru)
BR (1)	BRPI0810481B1 (ru)
CA (1)	CA2682677A1 (ru)
CL (2)	CL2008001128A1 (ru)
DK (1)	DK2137306T3 (ru)
EA (1)	EA017305B1 (ru)
ES (1)	ES2550362T3 (ru)
IL (1)	IL201018A0 (ru)
MX (1)	MX2009011256A (ru)
WO (1)	WO2008128975A1 (ru)

Families Citing this family (21)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6730832B1 (en)	2001-09-10	2004-05-04	Luis Mayan Dominguez	High threonine producing lines of Nicotiana tobacum and methods for producing
US7666652B2 (en)	2007-03-09	2010-02-23	Novozymes A/S	Asparaginases
EA018424B1 (ru)	2007-04-20	2013-07-30	ДСМ АйПи АССЕТС Б.В.	Варианты фермента аспарагиназы и их применение
US20110129569A1 (en)	2009-11-26	2011-06-02	Dsm Ip Assets B.V.	Method to produce fried vegetable products
US20120100249A1 (en) *	2010-04-27	2012-04-26	Dsm Ip Assets B.V.	Novel asparaginase enzyme
WO2012007192A1 (en) *	2010-07-14	2012-01-19	Nestec S.A.	Asparaginase from basidiomycetes
US9057087B2 (en)	2010-11-19	2015-06-16	Novozymes North America, Inc.	Processes of producing a fermentation product
WO2012158320A1 (en)	2011-05-13	2012-11-22	Baker Hughes Incorporated	Method of using asparaginase as a polyacrylamide enzyme breaker
BR112014006735B1 (pt) *	2011-09-21	2021-06-22	Reynolds Technologies, Inc	Método de produção de uma planta de tabaco modificada e produto de tabaco
US8716571B2 (en)	2011-09-21	2014-05-06	Reynolds Technologies, Inc.	Tobacco having reduced amounts of amino acids and methods for producing such lines
US9137958B2 (en)	2012-02-08	2015-09-22	Reynolds Technologies, Inc.	Tobacco having altered amounts of environmental contaminants
PL2884857T3 (pl) *	2012-08-17	2017-07-31	Novozymes A/S	Sposób wytwarzania produktu żywnościowego
US9828595B2 (en) *	2012-08-17	2017-11-28	Novozymes A/S	Thermostable asparaginase variants and polynucleotides encoding same
CN106414789A (zh)	2013-11-21	2017-02-15	恩特格里斯公司	用于在等离子体系统中使用的室组件的表面涂层
WO2016001894A1 (en)	2014-07-04	2016-01-07	West Systems Srl	Method and composition to reduce the formation of acrylamide in fresh or pre-fried foods to be subjected to heat treatment
CA2991325A1 (en) *	2015-07-07	2017-01-12	Renaissance Bioscience Corp.	Development of an asparagine-reducing yeast by adaptive evolution and uses thereof to reduce acrylamide formation
WO2019083794A1 (en)	2017-10-27	2019-05-02	Pfenex Inc.	PROCESS FOR PRODUCING EAR ASPARAGINASE. RECOMBINED COLI
JP7784804B2 (ja)	2017-10-27	2025-12-12	フェネックスインク．	組み換えｅｒｗｉｎｉａアスパラギナーゼの製造のための方法
US20210299233A1 (en)	2018-07-12	2021-09-30	The Children's Medical Center Corporation	Method for treating cancer
WO2022211829A1 (en)	2021-03-30	2022-10-06	Jazz Pharmaceuticals Ireland Ltd.	Dosing of recombinant l-asparaginase
CN119630280A (zh)	2022-05-14	2025-03-14	诺维信公司	用于预防、处理、抑制和/或消除植物病原性侵染和感染的组合物和方法

Family Cites Families (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP3819540B2 (ja) *	1996-06-07	2006-09-13	株式会社林原生物化学研究所	Ｌ−アスパラギナーゼ活性を有する哺乳類由来のポリペプチド
US7037540B2 (en)	2002-09-19	2006-05-02	Frito-Lay North America, Inc.	Method for reducing acrylamide formation in thermally processed foods
US7524519B2 (en) *	2002-09-20	2009-04-28	The Procter & Gamble Company	Method for reducing acrylamide in foods, foods having reduced levels of acrylamide, and article of commerce
ES2533469T3 (es)	2002-10-11	2015-04-10	Novozymes A/S	Método de preparación de un producto tratado con calor
US20040101607A1 (en)	2002-11-22	2004-05-27	The Procter & Gamble Company	Method for reducing acrylamide in foods, foods having reduced levels of acrylamide, and article of commerce
US8105815B2 (en)	2002-12-19	2012-01-31	Dsm Ip Assets B.V.	Asparaginase and its use in food production

2008
- 2008-04-17 WO PCT/EP2008/054693 patent/WO2008128975A1/en not_active Ceased
- 2008-04-17 ES ES08736346.1T patent/ES2550362T3/es active Active
- 2008-04-17 EP EP08736346.1A patent/EP2137306B1/en active Active
- 2008-04-17 US US12/596,705 patent/US20100136169A1/en not_active Abandoned
- 2008-04-17 CA CA002682677A patent/CA2682677A1/en not_active Abandoned
- 2008-04-17 JP JP2010503509A patent/JP2010524448A/ja active Pending
- 2008-04-17 EA EA200901432A patent/EA017305B1/ru not_active IP Right Cessation
- 2008-04-17 DK DK08736346.1T patent/DK2137306T3/en active
- 2008-04-17 MX MX2009011256A patent/MX2009011256A/es not_active Application Discontinuation
- 2008-04-17 AU AU2008240797A patent/AU2008240797A1/en not_active Abandoned
- 2008-04-17 BR BRPI0810481-6A patent/BRPI0810481B1/pt active IP Right Grant
- 2008-04-18 CL CL200801128A patent/CL2008001128A1/es unknown
- 2008-04-18 AR ARP080101640A patent/AR066410A1/es unknown
- 2008-04-18 CL CL200801129A patent/CL2008001129A1/es unknown
2009
- 2009-09-17 IL IL201018A patent/IL201018A0/en unknown
2011
- 2011-08-29 US US13/137,597 patent/US8323948B2/en active Active
2012
- 2012-09-14 US US13/618,606 patent/US20130023029A1/en not_active Abandoned

Also Published As

Publication number	Publication date
IL201018A0 (en)	2011-08-01
US20100136169A1 (en)	2010-06-03
JP2010524448A (ja)	2010-07-22
CL2008001128A1 (es)	2008-06-13
EP2137306A1 (en)	2009-12-30
US20130023029A1 (en)	2013-01-24
EP2137306B1 (en)	2015-07-29
WO2008128975A1 (en)	2008-10-30
US8323948B2 (en)	2012-12-04
BRPI0810481A2 (pt)	2014-10-07
EA200901432A1 (ru)	2010-04-30
MX2009011256A (es)	2009-11-05
CA2682677A1 (en)	2008-10-30
AR066410A1 (es)	2009-08-19
BRPI0810481B1 (pt)	2022-05-17
EA017305B1 (ru)	2012-11-30
CL2008001129A1 (es)	2008-06-13
AU2008240797A1 (en)	2008-10-30
DK2137306T3 (en)	2015-10-26
US20120045549A1 (en)	2012-02-23

Publication	Publication Date	Title
ES2550362T3 (es)	2015-11-06	Nuevas asparaginasas y usos de las mismas
ES2549775T3 (es)	2015-11-02	Variantes de glucósido hidrolasas
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LUO et al.	1999	The human Prp8 protein is a component of both U2-and U12-dependent spliceosomes
ES2552793T3 (es)	2015-12-02	Variantes de SAP y su uso
Faraldo et al.	1992	Sequence of the S-layer gene of Thermus thermophilus HB8 and functionality of its promoter in Escherichia coli
Berglund et al.	1998	The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequence
Cerritelli et al.	1998	Cloning, expression, and mapping of ribonucleases H of human and mouse related to bacterial RNase HI
CA2118071A1 (en)	1995-04-29	Dna encoding limonene synthase from mentha spicata
Kato et al.	1993	RecA protein from an extremely thermophilic bacterium, Thermus thermophilus HB8
Seither et al.	1996	Molecular cloning of RPA2, the gene encoding the second largest subunit of mouse RNA polymerase I
Kolukisaoglu et al.	1993	Mosses do express conventional, distantly B‐type‐related phytochromes phytochrome of Physcomitrella patens (Hedw.)
ES2557633T3 (es)	2016-01-27	Ribonucleasa H modificada por ingeniería específica de secuencia y el método para determinar la preferencia de secuencia de proteínas de unión de híbrido de ADN-ARN
BR112012010537A2 (pt)	2016-11-29	"clonagem, expressão e uso de fosfolipases ácidas"
WO2026011782A1 (zh)	2026-01-15	抑制FXI基因表达的siRNA的制备方法
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WO2025007044A1 (en)	2025-01-02	Methods and compositions comprising iscb variants
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Yamamoto et al.	2000	Effects of specific mutations in active site motifs of 2', 5'-oligoadenylate synthetase on enzymatic activity
Behammer et al.	1995	Flagellar structure and hyperthermophily: analysis of a single flagellin gene and its product in Aquifex pyrophilus
Feldmann et al.	1993	Single exchanges of amino acids in the basic region change the specificity of N-Myc
Nagasato et al.	2004	Characterization of centrin genes from Ochromonas danica (Chrysophyceae) and Scytosiphon lomentaria (Phaeophyceae)
ES2660341T3 (es)	2018-03-21	Dianas bacterianas de adquisición de hierro
Janes et al.	2000	Primary structure of myosin from the striated adductor muscle of the Atlantic scallop, Pecten maximus, and expression of the regulatory domain